A yeast BH3-only protein mediates the mitochondrial pathway of apoptosis
Open accessAbstract
Mitochondrial outer membrane permeabilization is a watershed event in the process of apoptosis, which is tightly regulated by a series of pro- and anti-apoptotic proteins belonging to the BCL-2 family, each characteristically possessing a BCL-2 homology domain 3 (BH3). Here, we identify a yeast protein (Ybh3p) that interacts with BCL-X(L) and harbours a functional BH3 domain. Upon lethal insult, Ybh3p translocates to mitochondria and triggers BH3 domain-dependent apoptosis. Ybh3p induces cell death and disruption of the mitochondrial transmembrane potential via the mitochondrial phosphate carrier Mir1p. Deletion of Mir1p and depletion of its human orthologue (SLC25A3/PHC) abolish stress-induced mitochondrial targeting of Ybh3p in yeast and that of BAX in human cells, respectively. Yeast cells lacking YBH3 display prolonged chronological and replicative lifespans and resistance to apoptosis induction. Thus, the yeast genome encodes a functional BH3 domain that induces cell death through phylogenetically conserved mechanisms.
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Deletion of YBH3 was reported to increase both replicative and chronological life span.
“Deletion of YBH3 was reported to increase both replicative and chronological life span (Buttner et al., 2011).”
From Programmed cell death in aging (2015) · cites this paper as Buttner et al., 2011
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References 56 · Cited by 133
- Authors
- Büttner, S., Ruli, D., Vögtle, F., Galluzzi, L., Moitzi, B., Eisenberg, T., Kepp, O., Habernig, L., Carmona‐Gutierrez, D., Rockenfeller, P., Laun, P., Breitenbach, M., Khoury, C., Fröhlich, K., Rechberger, G., Meisinger, C., Kroemer, G., & Madeo, F.
- Affiliations
- University of Graz (AT)
- University of Freiburg (DE)
- Université Paris-Sud (FR)
- University of Salzburg (AT)
- Inserm (FR)
- Corresponding author
- Kroemer, Guido
- Madeo, Frank
- ORCID
- Venue
- The EMBO Journal
- Published
- 2011-06-14
- Volume
- 30
- Issue
- 14
- Pages
- 2779-2792
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3160254
- OpenAlex
- W2168140776
- Cited by
- 133
- References
- 56
- Citations by year
- 2026: 2 · 2025: 1 · 2024: 6 · 2023: 5 · 2022: 3 · 2021: 5 · 2020: 7 · 2019: 5 · 2018: 6 · 2017: 14 · 2016: 16 · 2015: 10 · 2014: 7 · 2013: 15 · 2012: 25
- FWCI
- 6.89
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Commission
- Agence Nationale de la Recherche
- Austrian Science Fund (S9304-B05, S9302-B05, T 414, W 1226, W1226-B18)
- Ligue Contre le Cancer
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- BH3-only proteins, mitochondrial apoptosis, Bcl-xL, Bcl-2 family proteins, mitochondrial outer membrane permeabilization, SLC25A3, mitochondrial phosphate carrier, mitochondrial membrane potential, Bax, chronological lifespan, replicative lifespan, yeast
- MeSH terms
- Amino Acid Sequence, Animals, Bone Neoplasms, Cell Cycle, Flow Cytometry, Humans, Lung Neoplasms, Mitochondria, Molecular Sequence Data, Peptide Fragments, Proto-Oncogene Proteins, RNA, Messenger, Saccharomyces cerevisiae, Tumor Cells, Cultured, Blotting, Western, Signal Transduction, Apoptosis, Sequence Homology, Amino Acid, Reverse Transcriptase Polymerase Chain Reaction, Mitochondrial Proteins, Phosphate Transport Proteins, Saccharomyces cerevisiae Proteins, RNA, Small Interfering, Immunoprecipitation, Apoptosis Regulatory Proteins, bcl-X Protein, bcl-2-Associated X Protein, Mice, Membrane Potential, Mitochondrial
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